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20 results on '"Meotti, Flavia C."'

8. Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2

Author

Peskin, Alexander V., primary, Meotti, Flavia C., additional, Kean, Kelsey M., additional, Göbl, Christoph, additional, Peixoto, Albert Souza, additional, Pace, Paul E., additional, Horne, Christopher R., additional, Heath, Sarah G., additional, Crowther, Jennifer M., additional, Dobson, Renwick C.J., additional, Karplus, P. Andrew, additional, and Winterbourn, Christine C., additional

Published
2021
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17. Chemical Characterization of Urate Hydroperoxide, A Pro-oxidant Intermediate Generated by Urate Oxidation in Inflammatory and Photoinduced Processes

Author

Patrício, Eliziane S., primary, Prado, Fernanda M., additional, da Silva, Railmara P., additional, Carvalho, Larissa A. C., additional, Prates, Marcus V. C., additional, Dadamos, Tony, additional, Bertotti, Mauro, additional, Di Mascio, Paolo, additional, Kettle, Anthony J., additional, and Meotti, Flavia C., additional

Published
2015
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20. The SARS-CoV-2 Nsp3 macrodomain reverses PARP9/DTX3L-dependent ADP-ribosylation induced by interferon signaling.

Author

Cristina Russo, Lilian, Tomasin, Rebeka, Araújo Matos, Isaac, Carlos Manucci, Antonio, Sowa, Sven T., Dale, Katie, Caldecott, Keith W., Lehtiö, Lari, Schechtman, Deborah, Meotti, Flavia C., Bruni-Cardoso, Alexandre, and Carlos Hoch, Nicolas

Subjects
*POST-translational modification, *ADP-ribosylation, *COVID-19, *POLY ADP ribose, *INTERFERONS, *SARS-CoV-2, *CELL physiology, *DRUG development
Abstract

SARS-CoV-2 nonstructural protein 3 (Nsp3) contains a macrodomain that is essential for coronavirus pathogenesis and is thus an attractive target for drug development. This macrodomain is thought to counteract the host interferon (IFN) response, an important antiviral signalling cascade, via the reversal of protein ADP-ribosylation, a posttranslational modification catalyzed by host poly(ADP-ribose) polymerases (PARPs). However, the main cellular targets of the coronavirus macrodomain that mediate this effect are currently unknown. Here, we use a robust immunofluorescence-based assay to show that activation of the IFN response induces ADP-ribosylation of host proteins and that ectopic expression of the SARSCoV- 2 Nsp3 macrodomain reverses this modification in human cells. We further demonstrate that this assay can be used to screen for on-target and cell-active macrodomain inhibitors. This IFN-induced ADP-ribosylation is dependent on PARP9 and its binding partner DTX3L, but surprisingly the expression of the Nsp3 macrodomain or the deletion of either PARP9 or DTX3L does not impair IFN signaling or the induction of IFNresponsive genes. Our results suggest that PARP9/DTX3Ldependent ADP-ribosylation is a downstream effector of the host IFN response and that the cellular function of the SARSCoV- 2 Nsp3 macrodomain is to hydrolyze this end product of IFN signaling, rather than to suppress the IFN response itself. [ABSTRACT FROM AUTHOR]

Published
2021
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